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  • 1
    ISSN: 1434-0879
    Keywords: Bladder outlet obstruction ; Mucosa ; Serosa ; Rabbit ; FT-IR ; ATR ; Protein secondary structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The biochemical composition of physiologically moist mucosa and serosa of rabbit bladder before and after bladder outlet obstruction was determined by means of FT-IR spectroscopy with the ATR method and second-derivative analysis. A predominantly β-sheet structure was found in the amide I band for mucosa and serosa before and after obstruction, but the random coil structure increased in both obstructed bladder samples. However, the major β-sheet structure associated with some α-helical structure in the amide II band of mucosa and serosa for non-obstructed bladder changed into a predominanly α-helical structure after bladder obstruction. The obstructed bladder serosa was more pronounced. The amount of glycoproteins doubled in the obstructed bladder serosa, but did not change in the bladder mucosa.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-1424
    Keywords: Folate compounds ; transport multiplicity L1210 cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Various independent kinetic criteria for indicating multiplicity of carrier-mediated entry of folate compounds into L1210 cell plasma membrane vesicles are studied. We find a marked inconsistency between values for influxK m andK ix in reciprocal experiments measuring competition between various folate compounds as well as inconsistent effects of transloading shown for 5-formyltetrahydrofolate influx, but not folic acid influx. These results argue strongly against a one-carrier model for transport of folate compounds. The most straightforward interpretation of our data is that two distinct transport systems mediate entry of folate compounds in L1210 plasma membrane vesicles. If a two-carrier model is correct, then our data indicate that one of the carriers has low capacity and high affinity for folate coenzymes and methotrexate. This system is apparently negligible as a transport route for folic acid. Transtimulation of initial influx by substrates of the low capacity system is obtained following transloading with coenzymes but not by transloading with folic acid. Our data indicate that the second folate transport system postulated by the two-carrier model has a low affinity for all the folate compounds studied. Nevertheless, the putative second system is significant, especially for folic acid transport, because it has a much higher capacity than the first transport system. In contrast to the first system, transloading with any of the folate compounds studied had no effect on initial influx mediated by the second folate transport system. The two systems are also differentially inhibited bypCMBS, DIDS and SITS and the influxV max for the high-affinity/low-capacity system was altered in a vesicle preparation derived from a methotrexate resistant L1210 cell line.
    Type of Medium: Electronic Resource
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